Molecular Determinants for the Self-Assembly of Elastin Peptides. (21st August 2014)

• Record Type: Journal Article
• Authors: Bochicchio, Brigida; Armenante, Maria Rosaria; Crudele, Maria Antonietta; Pepe, Antonietta
• Other Names: Lepedda Antonio Academic Editor.
• Is Part Of: Conference papers in science. Volume 2014(2014)
• Publication Date: 2014-08-21
• Subjects: Science -- Periodicals; Science; Periodicals; 600
• DOI: 10.1155/2014/214235
• Languages: English
• ISSNs: 2356-6108

Abstract

Abstract : Elastin and elastin-related peptides have great potential in the biomaterial field, because of their peculiar mechanical properties and spontaneous self-assembling behavior. Depending on their sequences and under appropriate experimental conditions, they are able to self-assemble in different fiber morphologies, including amyloid-like fibers. In this work, we will review recent data on elastin peptides derived from exon 30-coded domain of human tropoelastin. This domain has been shown to be fundamental for the correct assembly of elastin. However, the N-terminal region forms amyloid-like fibers, while the C-terminal fragment forms elastin-like fibers. A rationale for the varied aggregation pattern has been sought in the molecular structure of the peptides. Minimal differences in the sequences, adopting alternative conformations, are shown to be responsible for the observed data.